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Methods in Molecular Biology (Clifton, N.J.)|November 5, 2011
Fluorescence correlation spectroscopy and allostery: the case of GroELGabriel A Frank, Amnon Horovitz, Gilad Haran
Journal of Molecular Biology|October 1, 2016
Transient Kinetic Analysis of ATP Hydrolysis by the CCT/TRiC ChaperoninIlia Korobko, Michal Nadler-Holly, Amnon Horovitz
Journal of Molecular Biology|June 17, 2008
Concerted release of substrate domains from GroEL by ATP is demonstrated with FRETNiv Papo, Yakov Kipnis, Gilad Haran, et al.
Elife|July 28, 2020
Measuring protein stability in the GroEL chaperonin cage reveals massive destabilizationIlia Korobko, Hisham Mazal, Gilad Haran, et al.
Plos One|February 14, 2018
Comparative genomic analysis of mollicutes with and without a chaperonin systemDominik Schwarz, Orit Adato, Amnon Horovitz, et al.
Biophysical Journal|December 23, 2018
Contact Order Is a Determinant for the Dependence of GFP Folding on the Chaperonin GroELBoudhayan Bandyopadhyay, Tridib Mondal, Ron Unger, et al.
Proceedings of the National Academy of Sciences of the United States of America|March 16, 2007
Concerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none mannerYakov Kipnis, Niv Papo, Gilad Haran, et al.
Proceedings of the National Academy of Sciences of the United States of America|October 22, 2002
Phi value analysis of heterogeneity in pathways of allosteric transitions: Evidence for parallel pathways of ATP-induced conformational changes in a GroEL ringAmnon Horovitz, Amnon Amir, Oded Danziger, et al.
Proceedings of the National Academy of Sciences of the United States of America|November 21, 2022
A diminished hydrophobic effect inside the GroEL/ES cavity contributes to protein substrate destabilizationIlia Korobko, Robin Benjamin Eberle, Mousam Roy, et al.
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